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P00909 (TRPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan biosynthesis protein TrpCF

Including the following 2 domains:

  1. Indole-3-glycerol phosphate synthase
    Short name=IGPS
    EC=4.1.1.48
  2. N-(5'-phospho-ribosyl)anthranilate isomerase
    Short name=PRAI
    EC=5.3.1.24
Gene names
Name:trpC
Synonyms:trpF
Ordered Locus Names:b1262, JW1254
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. HAMAP-Rule MF_00134_B

Catalytic activity

N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_00134_B

1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP-Rule MF_00134_B

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_00134_B

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.

Subunit structure

Monomer.

Sequence similarities

In the N-terminal section; belongs to the TrpC family.

In the C-terminal section; belongs to the TrpF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Tryptophan biosynthesis protein TrpCF HAMAP-Rule MF_00134_B
PRO_0000154277

Regions

Region1 – 257257Indole-3-glycerol phosphate synthase HAMAP-Rule MF_00134_B
Region258 – 453196N-(5'-phosphoribosyl)anthranilate isomerase HAMAP-Rule MF_00134_B

Experimental info

Sequence conflict311Missing in CAA23673. Ref.3
Sequence conflict951Q → R in CAA23664. Ref.1
Sequence conflict951Q → R in AAA57299. Ref.1
Sequence conflict951Q → R in CAA23673. Ref.3
Sequence conflict2851Missing in CAA23673. Ref.3
Sequence conflict2941V → D in CAA23673. Ref.3
Sequence conflict3301A → V in CAA23664. Ref.1
Sequence conflict3301A → V in AAA57299. Ref.1
Sequence conflict3301A → V in CAA23673. Ref.3
Sequence conflict3991S → T in CAA23664. Ref.1
Sequence conflict3991S → T in AAA57299. Ref.1
Sequence conflict3991S → T in CAA23673. Ref.3
Sequence conflict3991S → T in AAB60033. Ref.4

Secondary structure

............................................................................................ 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00909 [UniParc].

Last modified March 19, 2014. Version 4.
Checksum: 09D5DA2353291F33

FASTA45349,492
        10         20         30         40         50         60 
MMQTVLAKIV ADKAIWVEAR KQQQPLASFQ NEVQPSTRHF YDALQGARTA FILECKKASP 

        70         80         90        100        110        120 
SKGVIRDDFD PARIAAIYKH YASAISVLTD EKYFQGSFNF LPIVSQIAPQ PILCKDFIID 

       130        140        150        160        170        180 
PYQIYLARYY QADACLLMLS VLDDDQYRQL AAVAHSLEMG VLTEVSNEEE QERAIALGAK 

       190        200        210        220        230        240 
VVGINNRDLR DLSIDLNRTR ELAPKLGHNV TVISESGINT YAQVRELSHF ANGFLIGSAL 

       250        260        270        280        290        300 
MAHDDLHAAV RRVLLGENKV CGLTRGQDAK AAYDAGAIYG GLIFVATSPR CVNVEQAQEV 

       310        320        330        340        350        360 
MAAAPLQYVG VFRNHDIADV VDKAKVLSLA AVQLHGNEEQ LYIDTLREAL PAHVAIWKAL 

       370        380        390        400        410        420 
SVGETLPARE FQHVDKYVLD NGQGGSGQRF DWSLLNGQSL GNVLLAGGLG ADNCVEAAQT 

       430        440        450 
GCAGLDFNSA VESQPGIKDA RLLASVFQTL RAY 

« Hide

References

« Hide 'large scale' references
[1]"Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions."
Christie G.E., Platt T.
J. Mol. Biol. 142:519-530(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium."
Horowitz H., van Arsdell J., Platt T.
J. Mol. Biol. 169:775-797(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 95 AND 399.
[3]"The complete nucleotide sequence of the tryptophan operon of Escherichia coli."
Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M.
Nucleic Acids Res. 9:6647-6668(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons."
Milkman R., Bridges M.M.
Genetics 133:455-468(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Deep coverage of the Escherichia coli proteome enables the assessment of false discovery rates in simple proteogenomic experiments."
Krug K., Carpy A., Behrends G., Matic K., Soares N.C., Macek B.
Mol. Cell. Proteomics 12:3420-3430(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-8.
Strain: K12 / BW25113.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0-A resolution."
Wilmanns M., Priestle J.P., Niermann T., Jansonius J.N.
J. Mol. Biol. 223:477-507(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 320.
[11]"Crystallization and structure solution at 4-A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue."
Wilmanns M., Schlagenhauf E., Fol B., Jansonius J.N.
Protein Eng. 3:173-180(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 258-453.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00366 Genomic DNA. Translation: CAA23664.1.
V00372 Genomic DNA. Translation: CAA23673.1.
J01714 Genomic DNA. Translation: AAA57299.1.
U23489 Genomic DNA. Translation: AAB60033.1.
U00096 Genomic DNA. Translation: AAC74344.3.
AP009048 Genomic DNA. Translation: BAA14794.1.
PIRGWEC. A64874.
RefSeqYP_489530.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JCMX-ray2.10P2-260[»]
1PIIX-ray2.00A2-453[»]
2KZHNMR-A256-385[»]
ProteinModelPortalP00909.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00909. 7 interactions.
STRING511145.b1262.

Proteomic databases

PaxDbP00909.
PRIDEP00909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74344; AAC74344; b1262.
BAA14794; BAA14794; BAA14794.
GeneID12931128.
KEGGecj:Y75_p1236.
eco:b1262.
PATRIC32117784. VBIEscCol129921_1312.

Organism-specific databases

EchoBASEEB1019.
EcoGeneEG11026. trpC.

Phylogenomic databases

eggNOGCOG0134.
HOGENOMHOG000280458.
KOK13498.
OMASFILECK.
OrthoDBEOG6WT8JX.
PhylomeDBP00909.
ProtClustDBPRK09427.

Enzyme and pathway databases

BioCycEcoCyc:PRAI-IGPS.
ECOL316407:JW1254-MONOMER.
MetaCyc:PRAI-IGPS.
UniPathwayUPA00035; UER00042.
UPA00035; UER00043.

Gene expression databases

GenevestigatorP00909.

Family and domain databases

Gene3D3.20.20.70. 2 hits.
HAMAPMF_00134_B. IGPS_B.
MF_00135. PRAI.
InterProIPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 2 hits.
PROSITEPS00614. IGPS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00909.
PROP00909.

Entry information

Entry nameTRPC_ECOLI
AccessionPrimary (citable) accession number: P00909
Secondary accession number(s): P78059, P78234, P94704
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 19, 2014
Last modified: April 16, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene